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Database: UniProt
Entry: A0A257R2F8_9PROT
LinkDB: A0A257R2F8_9PROT
Original site: A0A257R2F8_9PROT 
ID   A0A257R2F8_9PROT        Unreviewed;       467 AA.
AC   A0A257R2F8;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=Threonine synthase {ECO:0000256|ARBA:ARBA00018679};
DE            EC=4.2.3.1 {ECO:0000256|ARBA:ARBA00013028};
GN   ORFNames=B7Z76_12400 {ECO:0000313|EMBL:OYV54939.1};
OS   Acidiphilium sp. 20-67-58.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Acidiphilium.
OX   NCBI_TaxID=1970291 {ECO:0000313|EMBL:OYV54939.1, ECO:0000313|Proteomes:UP000216756};
RN   [1] {ECO:0000313|EMBL:OYV54939.1, ECO:0000313|Proteomes:UP000216756}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=20-67-58 {ECO:0000313|EMBL:OYV54939.1};
RA   Kantor R.S., Colenbrander Nelson T., Marshall S., Bennett D., Apte S.,
RA   Camacho D., Thomas B.C., Warren L.A., Banfield J.F.;
RT   "Lifting the veil on microbial sulfur biogeochemistry in mining
RT   wastewaters.";
RL   Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-homoserine = L-threonine + phosphate;
CC         Xref=Rhea:RHEA:10840, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57590, ChEBI:CHEBI:57926; EC=4.2.3.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00000051};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|PIRSR:PIRSR604450-51};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC       from L-aspartate: step 5/5. {ECO:0000256|ARBA:ARBA00004979}.
CC   -!- SIMILARITY: Belongs to the threonine synthase family.
CC       {ECO:0000256|ARBA:ARBA00005517}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OYV54939.1}.
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DR   EMBL; NCAS01000033; OYV54939.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A257R2F8; -.
DR   UniPathway; UPA00050; UER00065.
DR   Proteomes; UP000216756; Unassembled WGS sequence.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0004795; F:threonine synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd01560; Thr-synth_2; 1.
DR   Gene3D; 3.40.50.1100; -; 2.
DR   Gene3D; 3.90.1380.10; Threonine synthase, N-terminal domain; 1.
DR   InterPro; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS.
DR   InterPro; IPR029144; Thr_synth_N.
DR   InterPro; IPR037158; Thr_synth_N_sf.
DR   InterPro; IPR004450; Thr_synthase-like.
DR   InterPro; IPR001926; TrpB-like_PALP.
DR   InterPro; IPR036052; TrpB-like_PALP_sf.
DR   NCBIfam; TIGR00260; thrC; 1.
DR   PANTHER; PTHR42690; THREONINE SYNTHASE FAMILY MEMBER; 1.
DR   PANTHER; PTHR42690:SF1; THREONINE SYNTHASE-LIKE 2; 1.
DR   Pfam; PF00291; PALP; 1.
DR   Pfam; PF14821; Thr_synth_N; 1.
DR   SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
DR   PROSITE; PS00165; DEHYDRATASE_SER_THR; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR604450-51};
KW   Threonine biosynthesis {ECO:0000256|ARBA:ARBA00022697}.
FT   DOMAIN          2..81
FT                   /note="Threonine synthase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14821"
FT   DOMAIN          99..326
FT                   /note="Tryptophan synthase beta chain-like PALP"
FT                   /evidence="ECO:0000259|Pfam:PF00291"
FT   MOD_RES         113
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604450-51"
SQ   SEQUENCE   467 AA;  50212 MW;  1AE3A1B31E27980A CRC64;
     MRYVSTRGAA PSRDFDGVLL AGLAEDGGLF VPESWPTFSP AEWRALRGLP YAELAARVMA
     PFMTGGAIGF DDLQAITRAS YRGFDHAAVV PLVQLEPSLF VLELFHGPTL AFKDLALQVA
     GRLFDHVLAA RDERVTIVGA TSGDTGSAAI EACRDRLRVD IAILHPEGRT SEVQRRQMTT
     VNARNVLNIA LSGTFDDCQD LVKAMFADAP FRTELRLSAV NSINWARIAG QIPYFVAAAL
     ALGAPDRPVA VAVPTGNFGN ILAAWAARQM GLPIERFIVG SNANDILARF LAANDMRTAG
     VVETVSPSMD IQVSSNFERL LFEALGRDAP ATARTMTDFR ATGSMQVPSE VWQSVRRDFA
     GLALDDAATL AEIARIRAET GYMADPHTAI GIAAARAAAP VGVPVIAAAT AHPAKFPDAM
     HRAIGIRPGL PERLADLYHR DEHFVRAANS LGEVETLVRH FAHRNDA
//
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